PSS_SCHPO
ID PSS_SCHPO Reviewed; 240 AA.
AC O94584;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase;
GN Name=pps1; ORFNames=SPCC1442.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17905925; DOI=10.1128/ec.00300-07;
RA Matsuo Y., Fisher E., Patton-Vogt J., Marcus S.;
RT "Functional characterization of the fission yeast phosphatidylserine
RT synthase gene, pps1, reveals novel cellular functions for
RT phosphatidylserine.";
RL Eukaryot. Cell 6:2092-2101(2007).
RN [5]
RP FUNCTION.
RX PubMed=19366728; DOI=10.1242/jcs.046466;
RA Sajiki K., Hatanaka M., Nakamura T., Takeda K., Shimanuki M., Yoshida T.,
RA Hanyu Y., Hayashi T., Nakaseko Y., Yanagida M.;
RT "Genetic control of cellular quiescence in S. pombe.";
RL J. Cell Sci. 122:1418-1429(2009).
CC -!- FUNCTION: Phosphatidylserine synthase involved in the regulation of
CC processes such as cell morphology, cytokinesis, actin cytoskeleton, and
CC cell wall remodeling and integrity. Also plays a role in the
CC physiological adaptations required for stationary-phase survival.
CC {ECO:0000269|PubMed:17905925, ECO:0000269|PubMed:19366728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC Evidence={ECO:0000269|PubMed:17905925};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 1/2.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Cytoplasmic vesicle membrane. Note=During log-phase
CC growth, concentrates at the cell and nuclear peripheries as well
CC endoplasmic reticulum membranes, while in stationary-phase cells, is
CC redistributed to unusual cytoplasmic structures of unknown origin.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21446.2; -; Genomic_DNA.
DR PIR; T40977; T40977.
DR RefSeq; NP_588326.2; NM_001023317.2.
DR AlphaFoldDB; O94584; -.
DR SMR; O94584; -.
DR BioGRID; 275488; 2.
DR STRING; 4896.SPCC1442.12.1; -.
DR PaxDb; O94584; -.
DR EnsemblFungi; SPCC1442.12.1; SPCC1442.12.1:pep; SPCC1442.12.
DR GeneID; 2538911; -.
DR KEGG; spo:SPCC1442.12; -.
DR PomBase; SPCC1442.12; pps1.
DR VEuPathDB; FungiDB:SPCC1442.12; -.
DR eggNOG; ENOG502QPJG; Eukaryota.
DR HOGENOM; CLU_049944_5_0_1; -.
DR InParanoid; O94584; -.
DR OMA; CGMISKS; -.
DR UniPathway; UPA00558; UER00615.
DR PRO; PR:O94584; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IDA:PomBase.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; EXP:PomBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:PomBase.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:PomBase.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IMP:PomBase.
DR GO; GO:0007009; P:plasma membrane organization; IMP:PomBase.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR InterPro; IPR016271; CDP-diaglyc--ser_O-PTrfase_fun.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000852; Phosphatidylserine_synth_fun; 1.
DR TIGRFAMs; TIGR00473; pssA; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..240
FT /note="CDP-diacylglycerol--serine O-
FT phosphatidyltransferase"
FT /id="PRO_0000318107"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 240 AA; 26525 MW; 855D8E05FCD53A4C CRC64;
MVRSRVSPGL KLQSDASNQS NDKENKLLAY VNDNRHFSLI RALHLADLIT LMNGFCGVMS
IFSSLRYCLS GQQSAFHLWN AMYFMPFALF FDFLDGKVAR WRGKSSLMGQ ELDSLADLIS
FGVSPAVFAF CCGFQTFLDT VILSLFVLCG LTRLARFNVS VNSIPKDGSG KSQFFEGTPI
PTTLSLVTVC GVCILKGKTH ENLPWGEWCG NTPFAFHPLV VLFVLSGIAM TSKKLKVPKI
